The monooxygenase enzyme from the fungus Cunninghamella bainieri will be purified by various chromatographic techniques. The binding of oxygen, carbon monoxide and organic substrates by the enzyme will be studied. The nature of the ligands which bind metal at the active site to the enzyme will be investigated since this formation may explain the unususal spectral properties of the enzyme-carbon monoxide complex and the ability of the enzyme to both bind and activate oxygen. The structure of the active site of the enzyme will be investigated and compared with that observed for the P-450's from mammalian and microbial sources. The cytochrome c reductase enzyme which appears to be essential for the action of the fungal monooxygenase will also be characterized.